Full text data of AHSA1
AHSA1
(C14orf3)
[Confidence: low (only semi-automatic identification from reviews)]
Activator of 90 kDa heat shock protein ATPase homolog 1; AHA1 (p38)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Activator of 90 kDa heat shock protein ATPase homolog 1; AHA1 (p38)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95433
ID AHSA1_HUMAN Reviewed; 338 AA.
AC O95433; B2R9L2; Q96IL6; Q9P060;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Activator of 90 kDa heat shock protein ATPase homolog 1;
DE Short=AHA1;
DE AltName: Full=p38;
GN Name=AHSA1; Synonyms=C14orf3; ORFNames=HSPC322;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E.,
RA Scott H.S.;
RT "Isolation of a novel gene underexpressed in Down syndrome.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-338.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP INTERACTION WITH VSV G, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11554768; DOI=10.1006/bbrc.2001.5621;
RA Sevier C.S., Machamer C.E.;
RT "p38: a novel protein that associates with the vesicular stomatitis
RT virus glycoprotein.";
RL Biochem. Biophys. Res. Commun. 287:574-582(2001).
RN [9]
RP INTERACTION WITH HSPCA, MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=12504007; DOI=10.1016/S1097-2765(02)00785-2;
RA Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K.,
RA Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R.,
RA Cramer R., Mollapour M., Workman P., Piper P.W., Pearl L.H.,
RA Prodromou C.;
RT "Activation of the ATPase activity of hsp90 by the stress-regulated
RT cochaperone aha1.";
RL Mol. Cell 10:1307-1318(2002).
RN [10]
RP INTERACTION WITH HSPCA.
RX PubMed=12604615; DOI=10.1074/jbc.M212761200;
RA Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
RT "Aha1 binds to the middle domain of Hsp90, contributes to client
RT protein activation, and stimulates the ATPase activity of the
RT molecular chaperone.";
RL J. Biol. Chem. 278:17228-17235(2003).
RN [11]
RP INTERACTION WITH GCH1.
RX PubMed=16696853; DOI=10.1111/j.1471-4159.2006.03836.x;
RA Swick L., Kapatos G.;
RT "A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein
RT interactions.";
RL J. Neurochem. 97:1447-1455(2006).
RN [12]
RP INTERACTION WITH SRPK1.
RX PubMed=19240134; DOI=10.1101/gad.1752109;
RA Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
RT "Regulation of SR protein phosphorylation and alternative splicing by
RT modulating kinetic interactions of SRPK1 with molecular chaperones.";
RL Genes Dev. 23:482-495(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-3 AND LYS-212, MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP STRUCTURE BY NMR OF 204-335.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the C-terminal domain of human activator of
RT 90 kDa heat shock protein ATPase homolog 1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Cochaperone that stimulates HSP90 ATPase activity (By
CC similarity). May affect a step in the endoplasmic reticulum to
CC Golgi trafficking.
CC -!- SUBUNIT: Interacts with HSPCA/HSP90 and with the cytoplasmic tail
CC of the vesicular stomatitis virus glycoprotein (VSV G). Interacts
CC with GCH1. Interacts with SRPK1.
CC -!- INTERACTION:
CC P30793:GCH1; NbExp=3; IntAct=EBI-448610, EBI-958183;
CC P07900:HSP90AA1; NbExp=4; IntAct=EBI-448610, EBI-296047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum.
CC Note=May transiently interact with the endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues, including
CC brain, heart, skeletal muscle and kidney and, at lower levels,
CC liver and placenta.
CC -!- INDUCTION: By heat shock and treatment with the HSP90 inhibitor
CC 17-demethoxygeldanamycin (17AAG).
CC -!- SIMILARITY: Belongs to the AHA1 family.
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DR EMBL; AJ243310; CAB45684.1; -; mRNA.
DR EMBL; AF164791; AAF80755.1; -; mRNA.
DR EMBL; AK313824; BAG36559.1; -; mRNA.
DR EMBL; AF111168; AAD09623.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81291.1; -; Genomic_DNA.
DR EMBL; BC000321; AAH00321.1; -; mRNA.
DR EMBL; BC007398; AAH07398.2; -; mRNA.
DR EMBL; AF161440; AAF29000.1; -; mRNA.
DR PIR; JC7769; JC7769.
DR RefSeq; NP_036243.1; NM_012111.2.
DR UniGene; Hs.204041; -.
DR PDB; 1X53; NMR; -; A=204-335.
DR PDBsum; 1X53; -.
DR ProteinModelPortal; O95433; -.
DR SMR; O95433; 25-146, 204-335.
DR IntAct; O95433; 10.
DR MINT; MINT-5002315; -.
DR STRING; 9606.ENSP00000216479; -.
DR PhosphoSite; O95433; -.
DR REPRODUCTION-2DPAGE; IPI00030706; -.
DR PaxDb; O95433; -.
DR PeptideAtlas; O95433; -.
DR PRIDE; O95433; -.
DR Ensembl; ENST00000216479; ENSP00000216479; ENSG00000100591.
DR GeneID; 10598; -.
DR KEGG; hsa:10598; -.
DR UCSC; uc001xtw.3; human.
DR CTD; 10598; -.
DR GeneCards; GC14P077924; -.
DR HGNC; HGNC:1189; AHSA1.
DR HPA; CAB006244; -.
DR HPA; HPA000903; -.
DR MIM; 608466; gene.
DR neXtProt; NX_O95433; -.
DR PharmGKB; PA25515; -.
DR eggNOG; COG5580; -.
DR HOGENOM; HOG000242852; -.
DR HOVERGEN; HBG065806; -.
DR InParanoid; O95433; -.
DR OMA; WTEKNAT; -.
DR PhylomeDB; O95433; -.
DR ChiTaRS; AHSA1; human.
DR EvolutionaryTrace; O95433; -.
DR GeneWiki; AHSA1; -.
DR GenomeRNAi; 10598; -.
DR NextBio; 40246; -.
DR PRO; PR:O95433; -.
DR ArrayExpress; O95433; -.
DR Bgee; O95433; -.
DR CleanEx; HS_AHSA1; -.
DR Genevestigator; O95433; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:MGI.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0006950; P:response to stress; ISS:UniProtKB.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR013538; Activator_of_Hsp90_ATPase.
DR InterPro; IPR015310; AHSA1_N.
DR InterPro; IPR023393; START-like_dom.
DR Pfam; PF09229; Aha1_N; 1.
DR Pfam; PF08327; AHSA1; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SUPFAM; SSF103111; SSF103111; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
KW Endoplasmic reticulum; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 338 Activator of 90 kDa heat shock protein
FT ATPase homolog 1.
FT /FTId=PRO_0000215820.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 N6-acetyllysine.
FT MOD_RES 193 193 Phosphoserine.
FT MOD_RES 212 212 N6-acetyllysine.
FT CONFLICT 67 68 EA -> CL (in Ref. 7; AAF29000).
FT STRAND 206 217
FT HELIX 219 225
FT HELIX 229 235
FT TURN 253 256
FT STRAND 261 265
FT TURN 266 268
FT STRAND 269 276
FT STRAND 285 290
FT STRAND 298 308
FT HELIX 309 317
FT TURN 318 323
FT HELIX 324 330
SQ SEQUENCE 338 AA; 38274 MW; E6B686DDD8D7D729 CRC64;
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ NEEGKCEVTE
VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS
VSLAKDEPDT NLVALMKEEG VKLLREAMGI YISTLKTEFT QGMILPTMNG ESVDPVGQPA
LKTEERKAKP APSKTQARPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA
TLEADRGGKF HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF
//
ID AHSA1_HUMAN Reviewed; 338 AA.
AC O95433; B2R9L2; Q96IL6; Q9P060;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Activator of 90 kDa heat shock protein ATPase homolog 1;
DE Short=AHA1;
DE AltName: Full=p38;
GN Name=AHSA1; Synonyms=C14orf3; ORFNames=HSPC322;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E.,
RA Scott H.S.;
RT "Isolation of a novel gene underexpressed in Down syndrome.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-338.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP INTERACTION WITH VSV G, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11554768; DOI=10.1006/bbrc.2001.5621;
RA Sevier C.S., Machamer C.E.;
RT "p38: a novel protein that associates with the vesicular stomatitis
RT virus glycoprotein.";
RL Biochem. Biophys. Res. Commun. 287:574-582(2001).
RN [9]
RP INTERACTION WITH HSPCA, MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=12504007; DOI=10.1016/S1097-2765(02)00785-2;
RA Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K.,
RA Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R.,
RA Cramer R., Mollapour M., Workman P., Piper P.W., Pearl L.H.,
RA Prodromou C.;
RT "Activation of the ATPase activity of hsp90 by the stress-regulated
RT cochaperone aha1.";
RL Mol. Cell 10:1307-1318(2002).
RN [10]
RP INTERACTION WITH HSPCA.
RX PubMed=12604615; DOI=10.1074/jbc.M212761200;
RA Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
RT "Aha1 binds to the middle domain of Hsp90, contributes to client
RT protein activation, and stimulates the ATPase activity of the
RT molecular chaperone.";
RL J. Biol. Chem. 278:17228-17235(2003).
RN [11]
RP INTERACTION WITH GCH1.
RX PubMed=16696853; DOI=10.1111/j.1471-4159.2006.03836.x;
RA Swick L., Kapatos G.;
RT "A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein
RT interactions.";
RL J. Neurochem. 97:1447-1455(2006).
RN [12]
RP INTERACTION WITH SRPK1.
RX PubMed=19240134; DOI=10.1101/gad.1752109;
RA Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
RT "Regulation of SR protein phosphorylation and alternative splicing by
RT modulating kinetic interactions of SRPK1 with molecular chaperones.";
RL Genes Dev. 23:482-495(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-3 AND LYS-212, MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP STRUCTURE BY NMR OF 204-335.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the C-terminal domain of human activator of
RT 90 kDa heat shock protein ATPase homolog 1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Cochaperone that stimulates HSP90 ATPase activity (By
CC similarity). May affect a step in the endoplasmic reticulum to
CC Golgi trafficking.
CC -!- SUBUNIT: Interacts with HSPCA/HSP90 and with the cytoplasmic tail
CC of the vesicular stomatitis virus glycoprotein (VSV G). Interacts
CC with GCH1. Interacts with SRPK1.
CC -!- INTERACTION:
CC P30793:GCH1; NbExp=3; IntAct=EBI-448610, EBI-958183;
CC P07900:HSP90AA1; NbExp=4; IntAct=EBI-448610, EBI-296047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum.
CC Note=May transiently interact with the endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues, including
CC brain, heart, skeletal muscle and kidney and, at lower levels,
CC liver and placenta.
CC -!- INDUCTION: By heat shock and treatment with the HSP90 inhibitor
CC 17-demethoxygeldanamycin (17AAG).
CC -!- SIMILARITY: Belongs to the AHA1 family.
CC -----------------------------------------------------------------------
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DR EMBL; AJ243310; CAB45684.1; -; mRNA.
DR EMBL; AF164791; AAF80755.1; -; mRNA.
DR EMBL; AK313824; BAG36559.1; -; mRNA.
DR EMBL; AF111168; AAD09623.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81291.1; -; Genomic_DNA.
DR EMBL; BC000321; AAH00321.1; -; mRNA.
DR EMBL; BC007398; AAH07398.2; -; mRNA.
DR EMBL; AF161440; AAF29000.1; -; mRNA.
DR PIR; JC7769; JC7769.
DR RefSeq; NP_036243.1; NM_012111.2.
DR UniGene; Hs.204041; -.
DR PDB; 1X53; NMR; -; A=204-335.
DR PDBsum; 1X53; -.
DR ProteinModelPortal; O95433; -.
DR SMR; O95433; 25-146, 204-335.
DR IntAct; O95433; 10.
DR MINT; MINT-5002315; -.
DR STRING; 9606.ENSP00000216479; -.
DR PhosphoSite; O95433; -.
DR REPRODUCTION-2DPAGE; IPI00030706; -.
DR PaxDb; O95433; -.
DR PeptideAtlas; O95433; -.
DR PRIDE; O95433; -.
DR Ensembl; ENST00000216479; ENSP00000216479; ENSG00000100591.
DR GeneID; 10598; -.
DR KEGG; hsa:10598; -.
DR UCSC; uc001xtw.3; human.
DR CTD; 10598; -.
DR GeneCards; GC14P077924; -.
DR HGNC; HGNC:1189; AHSA1.
DR HPA; CAB006244; -.
DR HPA; HPA000903; -.
DR MIM; 608466; gene.
DR neXtProt; NX_O95433; -.
DR PharmGKB; PA25515; -.
DR eggNOG; COG5580; -.
DR HOGENOM; HOG000242852; -.
DR HOVERGEN; HBG065806; -.
DR InParanoid; O95433; -.
DR OMA; WTEKNAT; -.
DR PhylomeDB; O95433; -.
DR ChiTaRS; AHSA1; human.
DR EvolutionaryTrace; O95433; -.
DR GeneWiki; AHSA1; -.
DR GenomeRNAi; 10598; -.
DR NextBio; 40246; -.
DR PRO; PR:O95433; -.
DR ArrayExpress; O95433; -.
DR Bgee; O95433; -.
DR CleanEx; HS_AHSA1; -.
DR Genevestigator; O95433; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:MGI.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0006950; P:response to stress; ISS:UniProtKB.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR013538; Activator_of_Hsp90_ATPase.
DR InterPro; IPR015310; AHSA1_N.
DR InterPro; IPR023393; START-like_dom.
DR Pfam; PF09229; Aha1_N; 1.
DR Pfam; PF08327; AHSA1; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SUPFAM; SSF103111; SSF103111; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
KW Endoplasmic reticulum; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 338 Activator of 90 kDa heat shock protein
FT ATPase homolog 1.
FT /FTId=PRO_0000215820.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 N6-acetyllysine.
FT MOD_RES 193 193 Phosphoserine.
FT MOD_RES 212 212 N6-acetyllysine.
FT CONFLICT 67 68 EA -> CL (in Ref. 7; AAF29000).
FT STRAND 206 217
FT HELIX 219 225
FT HELIX 229 235
FT TURN 253 256
FT STRAND 261 265
FT TURN 266 268
FT STRAND 269 276
FT STRAND 285 290
FT STRAND 298 308
FT HELIX 309 317
FT TURN 318 323
FT HELIX 324 330
SQ SEQUENCE 338 AA; 38274 MW; E6B686DDD8D7D729 CRC64;
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ NEEGKCEVTE
VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS
VSLAKDEPDT NLVALMKEEG VKLLREAMGI YISTLKTEFT QGMILPTMNG ESVDPVGQPA
LKTEERKAKP APSKTQARPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA
TLEADRGGKF HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF
//
MIM
608466
*RECORD*
*FIELD* NO
608466
*FIELD* TI
*608466 ACTIVATOR OF HEAT-SHOCK 90-KD PROTEIN ATPase 1; AHSA1
;;AHA1
*FIELD* TX
CLONING
read more
The vesicular stomatitis virus glycoprotein (VSVG) is a model
transmembrane glycoprotein used to study the exocytotic pathway. Using
the protein-sorting motifs in the VSVG tail as bait in a yeast 2-hybrid
screen of a HeLa cell cDNA library, followed by EST database analysis,
Sevier and Machamer (2001) cloned AHSA1, which they called p38. The
deduced 338-amino acid protein has a calculated molecular mass of 38.3
kD. Northern blot analysis detected a 1.5-kb transcript in brain, heart,
skeletal muscle, and kidney; lower levels were detected in liver and
placenta. Expression was below the level of detection in colon, thymus,
spleen, small intestine, lung, and peripheral blood leukocytes. However,
the authors identified AHSA1 sequences in colon, thymus, small
intestine, lung, and blood EST databases, suggesting that AHSA1
expression is ubiquitous but variable. Western blot analysis detected
endogenous AHSA1 at an apparent molecular mass of 40 kD in HeLa cells.
AHSA1 was primarily found in the cytosolic fraction of HeLa cell
homogenates, with some in the microsomal membrane pellet.
Immunofluorescence microscopy revealed strong cytosolic staining. When
proteins were crosslinked prior to visualization, AHSA1 staining showed
a more reticular pattern, suggesting that the crosslinker may have
stabilized an association of AHSA1 with a tethering protein in the
endoplasmic reticulum membrane.
By searching databases for sequences similar to an S. cerevisiae Hsp90
(140571) suppressor, Hch1, Lotz et al. (2003) identified AHSA1. The
deduced protein contains a putative N-terminal domain that is homologous
to Hch1 and a putative C-terminal domain.
GENE FUNCTION
Lotz et al. (2003) determined that interaction of HSP90 and AHSA1
required a region of HSP90 that links its N-terminal and middle domains.
They found that AHSA1 stimulated the intrinsic ATPase activity of HSP90
5-fold.
Cystic fibrosis (CF; 219700) is an inherited childhood disease primarily
triggered by defective folding and export of the CFTR (606421) protein
from the endoplasmic reticulum (ER). Using proteomics to assess global
CFTR protein interactions, Wang et al. (2006) showed that HSP90
cochaperones modulated HSP90-dependent stability of CFTR protein folding
in the ER. Small interfering RNA-mediated partial silencing of the HSP90
cochaperone AHA1 in human embryonic kidney and lung cell lines rescued
delivery of the most common disease-causing ER-restricted CFTR
delta-F508 variant (602421.0001) to the cell surface. Wang et al. (2006)
proposed that failure of CFTR delta-F508 to achieve an energetically
favorable fold in response to steady-state dynamics of the chaperone
folding environment is responsible for the pathophysiology of CF.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AHSA1
gene to chromosome 14 (TMAP WI-15374).
*FIELD* RF
1. Lotz, G. P.; Lin, H.; Harst, A.; Obermann, W. M. J.: Aha1 binds
to the middle domain of Hsp90, contributes to client protein activation,
and stimulates the ATPase activity of the molecular chaperone. J.
Biol. Chem. 278: 17228-17235, 2003.
2. Sevier, C. S.; Machamer, C. E.: p38: a novel protein that associates
with the vesicular stomatitis virus glycoprotein. Biochem. Biophys.
Res. Commun. 287: 574-582, 2001.
3. Wang, X.; Venable, J.; LaPointe, P.; Hutt, D. M.; Koulov, A. V.;
Coppinger, J.; Gurkan, C.; Kellner, W.; Matteson, J.; Plutner, H.;
Riordan, J. R.; Kelly, J. W.; Yates, J. R., III; Balch, W. E.: Hsp90
cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic
fibrosis. Cell 803-815, 2006.
*FIELD* CN
Matthew B. Gross - updated: 5/7/2009
*FIELD* CD
Patricia A. Hartz: 2/16/2004
*FIELD* ED
alopez: 09/30/2009
wwang: 5/11/2009
mgross: 5/7/2009
mgross: 2/16/2004
*RECORD*
*FIELD* NO
608466
*FIELD* TI
*608466 ACTIVATOR OF HEAT-SHOCK 90-KD PROTEIN ATPase 1; AHSA1
;;AHA1
*FIELD* TX
CLONING
read more
The vesicular stomatitis virus glycoprotein (VSVG) is a model
transmembrane glycoprotein used to study the exocytotic pathway. Using
the protein-sorting motifs in the VSVG tail as bait in a yeast 2-hybrid
screen of a HeLa cell cDNA library, followed by EST database analysis,
Sevier and Machamer (2001) cloned AHSA1, which they called p38. The
deduced 338-amino acid protein has a calculated molecular mass of 38.3
kD. Northern blot analysis detected a 1.5-kb transcript in brain, heart,
skeletal muscle, and kidney; lower levels were detected in liver and
placenta. Expression was below the level of detection in colon, thymus,
spleen, small intestine, lung, and peripheral blood leukocytes. However,
the authors identified AHSA1 sequences in colon, thymus, small
intestine, lung, and blood EST databases, suggesting that AHSA1
expression is ubiquitous but variable. Western blot analysis detected
endogenous AHSA1 at an apparent molecular mass of 40 kD in HeLa cells.
AHSA1 was primarily found in the cytosolic fraction of HeLa cell
homogenates, with some in the microsomal membrane pellet.
Immunofluorescence microscopy revealed strong cytosolic staining. When
proteins were crosslinked prior to visualization, AHSA1 staining showed
a more reticular pattern, suggesting that the crosslinker may have
stabilized an association of AHSA1 with a tethering protein in the
endoplasmic reticulum membrane.
By searching databases for sequences similar to an S. cerevisiae Hsp90
(140571) suppressor, Hch1, Lotz et al. (2003) identified AHSA1. The
deduced protein contains a putative N-terminal domain that is homologous
to Hch1 and a putative C-terminal domain.
GENE FUNCTION
Lotz et al. (2003) determined that interaction of HSP90 and AHSA1
required a region of HSP90 that links its N-terminal and middle domains.
They found that AHSA1 stimulated the intrinsic ATPase activity of HSP90
5-fold.
Cystic fibrosis (CF; 219700) is an inherited childhood disease primarily
triggered by defective folding and export of the CFTR (606421) protein
from the endoplasmic reticulum (ER). Using proteomics to assess global
CFTR protein interactions, Wang et al. (2006) showed that HSP90
cochaperones modulated HSP90-dependent stability of CFTR protein folding
in the ER. Small interfering RNA-mediated partial silencing of the HSP90
cochaperone AHA1 in human embryonic kidney and lung cell lines rescued
delivery of the most common disease-causing ER-restricted CFTR
delta-F508 variant (602421.0001) to the cell surface. Wang et al. (2006)
proposed that failure of CFTR delta-F508 to achieve an energetically
favorable fold in response to steady-state dynamics of the chaperone
folding environment is responsible for the pathophysiology of CF.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AHSA1
gene to chromosome 14 (TMAP WI-15374).
*FIELD* RF
1. Lotz, G. P.; Lin, H.; Harst, A.; Obermann, W. M. J.: Aha1 binds
to the middle domain of Hsp90, contributes to client protein activation,
and stimulates the ATPase activity of the molecular chaperone. J.
Biol. Chem. 278: 17228-17235, 2003.
2. Sevier, C. S.; Machamer, C. E.: p38: a novel protein that associates
with the vesicular stomatitis virus glycoprotein. Biochem. Biophys.
Res. Commun. 287: 574-582, 2001.
3. Wang, X.; Venable, J.; LaPointe, P.; Hutt, D. M.; Koulov, A. V.;
Coppinger, J.; Gurkan, C.; Kellner, W.; Matteson, J.; Plutner, H.;
Riordan, J. R.; Kelly, J. W.; Yates, J. R., III; Balch, W. E.: Hsp90
cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic
fibrosis. Cell 803-815, 2006.
*FIELD* CN
Matthew B. Gross - updated: 5/7/2009
*FIELD* CD
Patricia A. Hartz: 2/16/2004
*FIELD* ED
alopez: 09/30/2009
wwang: 5/11/2009
mgross: 5/7/2009
mgross: 2/16/2004